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In vitro sulfation of catechol estrogens with guinea pig and rat liver homogenates has been investigated by means of high-performance liquid chromatography with electrochemical detection. When incubated in a neutral medium (pH 7.4) with the liver 105000 g supernatant fortified with 3'-phosphoadenosine-5'-phosphosulfate, 2-hydroxyestrone and 4-hydroxyestrone were transformed principally into the 2- and 4-sulfates, respectively. The 3-sulfate was formed, and decreasing amounts of the 2- and 4-sulfates were obtained, as the pH of the incubation medium was decreased. The pH effect on directive glucuronidation was also examined with catechol estrogens. The product ratio of the isomeric ring A glucuronides formed was not affected by the pH of the incubation medium.

Studies on high-performance liquid chromatography with electrochemical detection. The pH-dependency of enzymic sulfation of catechol estrogens.